Voprosy meditsinskoi khimii (ISSN 0042-8809)

Hydrogen peroxide- supported oxidation of substrates by flavocytochrome 2B4.

   
Shumyantseva V.V., Avdeenko Yu.L., Moskvitina T.L., Bulko T. V., Osipov A.N., Archakov A. I.
PubMed Id: 9845924
Year: 1998 vol: 44  issue:4  pages: 369-375
Abstract: Semisynthetic flavocytochromes, obtained by covalent binding ofriboflavins with cytochrome P450 2B4, were able to catalyse H2O2 -supportedaniline p-hydroxylation, amidopyrine N-demethylation and p-nitroanisoleO-dealkylation. Rates of these reactions were considerably higher than the rates ofcorresponding NAD(P)H-dependent reactions and comparable with H2O2 -dependentreactions, catalysed by cytochrome P450. Kinetic parameters (Km and kcat)of hydrogen peroxide-supported oxidation of aniline, amidopyrine and p-nitroanisolein the presence of flavocytochrome 2B4 were determined. Cyanide and SKF-525 A inhibited H2O2-dependent reactions of flavocytochrome 2B4. The intensity of luminolchemiluminescence in the presence of hydrogen peroxide was studied. Chemiluminescentresponse was shown to be influenced by cyanide ions and SKF 525 A. The difference inchemiluminescence intencity of cytochrome P450 2B4 and semisynthetic flavocytochrome 2B4was found.
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Reference: Shumyantseva V.V., Avdeenko Yu.L., Moskvitina T.L., Bulko T. V., Osipov A.N., Archakov A. I., Hydrogen peroxide- supported oxidation of substrates by flavocytochrome 2B4. , Voprosy meditsinskoi khimii, 1998, vol: 44(4), 369-375.
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